NDLI: Substitution of Isoleucine L177 by Histidine Affects the Pigment Composition and Properties of the Reaction Center of the Purple Bacterium Rhodobacter sphaeroides

Content Provider	Springer Nature Link
Author	Khatypov, R. A. Vasilieva, L. G. Fufina, T. Y. Bolgarina, T. I. Shuvalov, V. A.
Copyright Year	2005
Abstract	Using site-directed mutagenesis, we obtained the mutant of the purple bacterium Rhodobacter sphaeroides with Ile to His substitution at position 177 in the L-subunit of the photosynthetic reaction center (RC). The mutant strain forms stable and photochemically active RC complexes. Relative to the wild type RCs, the spectral and photochemical properties of the mutant RC differ significantly in the absorption regions corresponding to the primary donor P and the monomer bacteriochlorophyll (BChl) absorption. It is shown that the RC I(L177)H contains only three BChl molecules compared to four BChl molecules in the wild type RC. Considering the fact that the properties of both isolated and membrane-associated mutant RCs are similar, we conclude that the loss of a BChl molecule from the mutant RC is caused by the introduced mutation but not by the protein purification procedure. The new mutant missing one BChl molecule but still able to perform light-induced reactions forming the charge-separated state P+QA A − appears to be an interesting object to study the mechanisms of the first steps of the primary electron transfer in photosynthesis.
Starting Page	1256
Ending Page	1261
Page Count	6
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	70
Issue Number	11
e-ISSN	16083040
Language	English
Publisher	Nauka/Interperiodica
Publisher Date	2005-01-01
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	bacterial photosynthesis reaction centers photochemical charge separation site-directed mutagenesis Rhodobacter sphaeroides Biomedicine general Bioorganic Chemistry Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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Properties of mutant reaction centers of Rhodobacter sphaeroides with substitutions of histidine L153, the axial Mg2+ ligand of bacteriochlorophyll BA

Properties of Rhodobacter sphaeroides photosynthetic reaction center with double amino acid substitution I(L177)H+H(M182)L

Femtosecond charge separation in dry films of reaction centers of Rhodobacter sphaeroides and Chloroflexus aurantiacus

Mutant reaction centers of Rhodobacter sphaeroides I(L177)H with strongly bound bacteriochlorophyll a: Structural properties and pigment-protein interactions

Charge separation in Rhodobacter sphaeroides mutant reaction centers with increased midpoint potential of the primary electron donor

Primary processes of charge separation in reaction centers of YM210L/FM197Y and YM210L mutants of Rhodobacter sphaeroides

Examination of stability of mutant photosynthetic reaction center of Rhodobacter sphaeroides I(L177)H and determination of location of bacteriochlorophyll covalently bound to the protein

Coherent phenomena of charge separation in reaction centers of LL131H and LL131H/LM160H/FM197H mutants of Rhodobacter sphaeroides

Different effects of identical symmetry-related mutations near the bacteriochlorophyll dimer in the photosynthetic reaction center of Rhodobacter sphaeroides

Substitution of Isoleucine L177 by Histidine Affects the Pigment Composition and Properties of the Reaction Center of the Purple Bacterium Rhodobacter sphaeroides

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Substitution of Isoleucine L177 by Histidine Affects the Pigment Composition and Properties of the Reaction Center of the Purple Bacterium Rhodobacter sphaeroides